We plan to study, first, those physiochemical properties of proteins which depend on the secondary, tertiary or quaternary structure of the molecule, and second, to probe particular functional sites with techniques capable of resolution at the atomic level. In the first area, we are developing a technique in which proteins migrate in an inhomogeneous alternating electric field only because of their electric dipole moments analogous to the motion of proteins due to their net charge in electrophgresis. In dielectrophoresis, dipolar molecular are attracted to the region of maximum absolute electric field intensity, and at equilibrium, a concentration gradient is established which is proportional to the dipole moment. This gradient can be quantitatively measured through the change in capacitance of a suitable cell. In addition, we shall also measure the rate of build-up and of decay of the gradient. We thus should obtain information on the mobility, diffusion constant, and dipole moment, as well as the dependence of these quantities of frequency. Second, we are making T1 and T2 relaxation measurements of C13, O17, F19 and H1 nuclei as a probe of the effects of the location, binding, and kinetics of copper, and other transition metals, on proteins. BIBLIOGRAPHIC REFERENCES: M.E. Fabry and M. Eisenstadt, 1975, Water Exchange Between Red Cells and Plasma. Measurement by Nuclear Magnetic Relaxation. Biophysical J., 15:1101-1110.